Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P08515 (GST26_SCHJA)

Last modified June 16, 2009. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutathione S-transferase class-mu 26 kDa isozyme
      Short name=GST 26
    EC=2.5.1.18
Alternative name(s):
    Sj26 antigen
    SjGST
OrganismSchistosoma japonicum (Blood fluke)
Taxonomic identifier6182 [NCBI]
Taxonomic lineageEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.

Catalytic activity

RX + glutathione = HX + R-S-glutathione.

Subunit structure

Homodimer.

Miscellaneous

There are at least two isoenzymes of GST in S.japonicum.

Sequence similarities

Belongs to the GST superfamily. Mu family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Molecular functionTransferase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Molecular functionglutathione transferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 218217Glutathione S-transferase class-mu 26 kDa isozyme
PRO_0000185805

Regions

Domain2 – 8382GST N-terminal
Domain85 – 203119GST C-terminal

Sites

Active site71 By similarity

Secondary structure

................................. 218
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08515-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 5E2AC418BD0EF13F

FASTA21825,499
        10         20         30         40         50         60 
MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID 

        70         80         90        100        110        120 
GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV 

       130        140        150        160        170        180 
DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK 

       190        200        210 
KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPK 

« Hide

References

[1]"Mr 26,000 antigen of Schistosoma japonicum recognized by resistant WEHI 129/J mice is a parasite glutathione S-transferase."
Smith D.B., Davern K.M., Board P.G., Tiu W.U., Garcia E.G., Mitchell G.F.
Proc. Natl. Acad. Sci. U.S.A. 83:8703-8707(1986) [PubMed: 3095841] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Smith D.B., Davern K.M., Board P.G., Tiu W.U., Garcia E.G., Mitchell G.F.
Proc. Natl. Acad. Sci. U.S.A. 84:6541-6541(1987)
Cited for: SEQUENCE REVISION.
[3]"Expression of an enzymatically active parasite molecule in Escherichia coli: Schistosoma japonicum glutathione S-transferase."
Smith D.B., Rubira M.R., Simpson R.J., Davern K.M., Tiu W.U., Board P.G., Mitchell G.F.
Mol. Biochem. Parasitol. 27:249-256(1988) [PubMed: 3278228] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-15.
[4]"Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV."
Lim K., Ho J.X., Keeling K., Gilliland G.L., Ji X., Ruker F., Carter D.C.
Protein Sci. 3:2233-2244(1994) [PubMed: 7538846] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[5]"Crystal structures of a schistosomal drug and vaccine target: glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel."
McTigue M.A., Williams D.R., Tainer J.A.
J. Mol. Biol. 246:21-27(1995) [PubMed: 7853399] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

M14654 mRNA. Translation: AAB59203.1.
PIRA61514.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1B8XX-ray2.70A2-218[»]
1BG5X-ray2.60A1-218[»]
1DUGX-ray1.80A/B2-218[»]
1GNEX-ray2.50A1-218[»]
1GTAX-ray2.40A1-218[»]
1GTBX-ray2.60A1-218[»]
1M99X-ray2.30A1-218[»]
1M9AX-ray2.10A1-218[»]
1M9BX-ray2.60A1-218[»]
1U87X-ray3.50A1-218[»]
1U88X-ray3.50A/B1-218[»]
1UA5X-ray2.50A1-218[»]
1Y6EX-ray3.00A/B2-217[»]
3CRTX-ray1.90A1-214[»]
3CRUX-ray2.30A1-214[»]
3D0ZX-ray2.50A1-214[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.5.1.18. 1465.

Family and domain databases

InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00143. Glutathione.
DB01058. Praziquantel.

Entry information

Entry nameGST26_SCHJA
AccessionPrimary (citable) accession number: P08515
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 81 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents